IUCr journals

Structures of MauG in complex with quinol and quinone MADH

Complex between MauG (pink) and methylamine dehydrogenase (blue and green).

The bacterial enzyme methylamine dehydrogenase (MADH) contains a redox cofactor generated through the post-translational modification of two Trp residues. Biosynthesis of the tryptophan tryptophylquinone (TTQ) cofactor is completed by a di-heme enzyme, MauG. This article reports the structures of MauG in complex with MADH (the product) and quinol MADH (a catalytic intermediate). Although the overall structures were identical, the crystal forms were not. Changes in the redox state of the TTQ appear to alter flexibility at the interface with MauG, and ultimately crystal packing.

E. T. Yukl, L. M. R. Jensen, V. L. Davidson and C. M. Wilmot

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